ID A0A219AMQ7_9EURY Unreviewed; 343 AA.
AC A0A219AMQ7;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide mutase {ECO:0000256|HAMAP-Rule:MF_01929};
DE Short=N5-CAIR mutase {ECO:0000256|HAMAP-Rule:MF_01929};
DE EC=5.4.99.18 {ECO:0000256|HAMAP-Rule:MF_01929};
DE AltName: Full=5-(carboxyamino)imidazole ribonucleotide mutase {ECO:0000256|HAMAP-Rule:MF_01929};
GN Name=purE {ECO:0000256|HAMAP-Rule:MF_01929};
GN ORFNames=BGI41_02140 {ECO:0000313|EMBL:OWT33479.1};
OS Methanobrevibacter sp. 87.7.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=387957 {ECO:0000313|EMBL:OWT33479.1, ECO:0000313|Proteomes:UP000197485};
RN [1] {ECO:0000313|EMBL:OWT33479.1, ECO:0000313|Proteomes:UP000197485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.7 {ECO:0000313|EMBL:OWT33479.1,
RC ECO:0000313|Proteomes:UP000197485};
RA Yeoman C., Mosoni P., White B.;
RT "De novo assembly of methanobrevibacter sp 87.7.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of N5-carboxyaminoimidazole
CC ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide
CC (CAIR). {ECO:0000256|HAMAP-Rule:MF_01929}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + H(+) = 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate;
CC Xref=Rhea:RHEA:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:58730,
CC ChEBI:CHEBI:77657; EC=5.4.99.18; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01929};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole (N5-CAIR route): step 2/2.
CC {ECO:0000256|HAMAP-Rule:MF_01929}.
CC -!- SIMILARITY: Belongs to the AIR carboxylase family. Class I subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01929}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWT33479.1}.
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DR EMBL; MRCT01000024; OWT33479.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A219AMQ7; -.
DR OrthoDB; 9473at2157; -.
DR UniPathway; UPA00074; UER00943.
DR Proteomes; UP000197485; Unassembled WGS sequence.
DR GO; GO:0034023; F:5-(carboxyamino)imidazole ribonucleotide mutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1970; -; 2.
DR HAMAP; MF_01929; PurE_classI; 1.
DR InterPro; IPR033747; PurE_ClassI.
DR InterPro; IPR000031; PurE_dom.
DR InterPro; IPR024694; PurE_prokaryotes.
DR NCBIfam; TIGR01162; purE; 2.
DR PANTHER; PTHR23046:SF2; PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE; 1.
DR PANTHER; PTHR23046; PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE CATALYTIC SUBUNIT; 1.
DR Pfam; PF00731; AIRC; 2.
DR SMART; SM01001; AIRC; 2.
DR SUPFAM; SSF52255; N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE); 2.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01929};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_01929}.
FT DOMAIN 4..152
FT /note="PurE"
FT /evidence="ECO:0000259|SMART:SM01001"
FT DOMAIN 198..342
FT /note="PurE"
FT /evidence="ECO:0000259|SMART:SM01001"
FT BINDING 12
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01929"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01929"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01929"
SQ SEQUENCE 343 AA; 37844 MW; 7F0299E91525352D CRC64;
MNNPKVMIIL GSGSDIKIAE KCMNKLDELK ISYSLKISSA HRTYDKVKHD VLEGTKNGIE
VFIGIAGMSA HLPGVITAFT YRPVIGVPVE AKLDGLDALY STIQMPFPAP VATVGIDRGD
NAAILAAQII GTYDEKVREN VHYVRLSYKN KVYNSQEDII KDLDYKYLVK DFIPDDLEEI
EYHHRTPDVE VLSEEECPDI AVIPGSHSDI TIAKKLSTLL DRMKISYDLK VVSPIRHPKR
FQEYIYKMQN VKLFIAINGL SSQISGSIVG LSEKPVIGVP CDKELNGKDS LLSMVSMPPG
VPVGSVGINN GRNCAILAGE ILGISNKDIE ESLKRIKYKT ANL
//
